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Database: UniProt
Entry: R0LY21_ANAPL
LinkDB: R0LY21_ANAPL
Original site: R0LY21_ANAPL 
ID   R0LY21_ANAPL            Unreviewed;      1338 AA.
AC   R0LY21;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   Flags: Fragment;
GN   ORFNames=Anapl_08388 {ECO:0000313|EMBL:EOB05358.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB05358.1, ECO:0000313|Proteomes:UP000296049};
RN   [1] {ECO:0000313|Proteomes:UP000296049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23749191; DOI=10.1038/ng.2657;
RA   Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA   Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA   Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA   Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA   Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA   Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA   Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA   Rao M., Pitel F., Wang J., Li N.;
RT   "The duck genome and transcriptome provide insight into an avian influenza
RT   virus reservoir species.";
RL   Nat. Genet. 45:776-783(2013).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR   EMBL; KB742696; EOB05358.1; -; Genomic_DNA.
DR   Proteomes; UP000296049; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:InterPro.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR   CDD; cd20875; C1_ROCK2; 1.
DR   CDD; cd11638; HR1_ROCK2; 1.
DR   CDD; cd01242; PH_ROCK; 1.
DR   CDD; cd22250; ROCK_SBD; 1.
DR   CDD; cd05596; STKc_ROCK; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.20.5.730; Single helix bin; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020684; ROCK1/ROCK2.
DR   InterPro; IPR037311; ROCK2_HR1.
DR   InterPro; IPR015008; ROCK_Rho-bd_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR   PANTHER; PTHR22988:SF28; RHO-ASSOCIATED PROTEIN KINASE 2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08912; Rho_Binding; 1.
DR   PIRSF; PIRSF037568; Rho_kinase; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF103652; G protein-binding domain; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51860; REM_1; 1.
DR   PROSITE; PS51859; RHO_BD; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01207}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EOB05358.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          48..310
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          313..381
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          450..526
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          930..998
FT                   /note="RhoBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51859"
FT   DOMAIN          1101..1300
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1211..1266
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          462..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1296..1338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          592..977
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1007..1052
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        503..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1314..1331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        170
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037568-1"
FT   BINDING         77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037568-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EOB05358.1"
FT   NON_TER         1338
FT                   /evidence="ECO:0000313|EMBL:EOB05358.1"
SQ   SEQUENCE   1338 AA;  155894 MW;  91CAAE93493E5B74 CRC64;
     SFQDGLNSLV LDLDYPALRK NKNIDNFLNR YEKIVEKIRA LQMKAEDYDV VKVIGRGAFG
     EVQLVRHKMT QKVYAMKLLS KFEMIKRSDS AFFWEERDIM AFANSPWVVQ LFCAFQDDKY
     LYMVMEYMPG GDLVNLMSNY DVPEKWAKFY TAEVVLALDA IHSMGLIHRD VKPDNMLLDK
     YGHLKLADFG TCMKMDETGM VRCDTAVGTP DYISPEVLKS QGGDGYYGRE CDWWSVGVFL
     FEMLVGDTPF YADSLVGTYS KIMDHKNSLH FPDDVEISKH AKNLICAFLT DRDVRLGRNG
     VEEIKHHPFF KSDQWNWDNI RETAAPVVPE LSSDIDSSNF DDIEDDKGDV ETFPIPKAFV
     GNQLPFIGFT YYRDNLLLSD SSQSCRENES VQSSKNEFQK KISKLEEQLS NELQAKDELE
     QKYRSTNTRL EKIVKELDEE ITSRKNVESA VRQLEREKAL LQHKNTEYQR KAEHEADKKR
     NLENEVNSLK DQLEDLKKRN QNSQISNEKI NQLQRQASNS LLRSESDTAT RLRKNQTEST
     KQIQQLEANN RELQDKNCLL ENAKLKLEKD FLNLQSALES ERRDRSHGSE IISDLQGRIS
     SLEEEVKNGK SALAKLEMEK RQLQEKLTDL EKEKSNMEID MTYKFKVMQQ NLEQEEAEHK
     ATKARLADKN KIYESIEEAK SEAMKEMEKK LLEERALKQK VENRLLEAEK QRSMLDCDLK
     QSQQKINELL RQKDILNEDV KNLTLKIEQE TQKRCLTQND LKMQTQQVNT LKMSEKQLKQ
     ENNHLQEIKL SLEKQNNELR KERQDADGQM KELQDQLEAE QYFSTLYKTQ VRELKEECEE
     KTKLCKEIQQ KIQELQDERD SLAAQLEITL TKADSEQLAR SIAEEQYSDL EKEKIMKELE
     IKEMMARHKQ ELTEKDATIA SLEEANRTLT SDVANLANEK EELNNKLKEV QEQITKLKEE
     EANIGNIKAQ YEKQLLNERT LKTQAVNKLA EIMNRKGPVK RGADTDVRRK EKENRKLHME
     LKSEREKLTQ MMIKYQKEIN EMQAQIAEES QIRIELQMTL DSKDSDIEQL RSQLQSLHIG
     LDNSSIGSGP GDTETDDGFP ESRLEGWLSL PVRNNTKKFG WVKKYVIVSS KKILFYDSEQ
     DKEQSNPYMV LDIDKLFHVR PVTQTDVYRA DAKEIPRIFQ ILYANEGESK KEQEFPVEPM
     GEKSNYICHK GHEFIPTLYH FPTNCEACMK PLWHMFKPPP ALECRRCHIK CHKDHMDKKE
     EIIAPCKVYY DISTAKNLLL LANSTEEQQK WVSRLVKKIP KKPPAPDPFA RSSPRTSMKV
     QPNQSIRRPS RQLPPNKP
//
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